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Comparative Study
. 1999 Oct;181(19):6200-4.
doi: 10.1128/JB.181.19.6200-6204.1999.

Purification and characterization of a novel naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038

M J Larkin  1 , C C Allen, L A Kulakov, D A Lipscomb
Affiliations
Comparative Study

Purification and characterization of a novel naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038

M J Larkin et al. J Bacteriol. 1999 Oct.

Abstract

We report here the characterization of the catalytic component (ISP(NAR)) of a new naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038. The genes encoding the two subunits of ISP(NAR) are not homologous to their previously characterized counterparts in Pseudomonas. The deduced amino acid sequences have only 33 and 29% identity with the corresponding subunits in Pseudomonas putida NCIB 9816-4, for which the tertiary structure has been reported.

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Figures

FIG. 1
FIG. 1
Expression of NDO ISPNAR α and β subunits in protein extracts from Rhodococcus sp. strain NCIMB12038 grown on naphthalene (C), salicylate (D), and pyruvate (E). Purified ISPNAR α and β subunits are also shown (B and F). Size markers are low-molecular-weight standards (A and G) (Bio-Rad).
FIG. 2
FIG. 2
Amino acid sequence alignment of the ISPNAR α subunits of naphthalene dioxygenases of P. putida 9816-4 (NahAc) and Rhodococcus sp. strain NCIMB12038 (NarAa). Sequences were aligned by the CLUSTALW program, and manual corrections were introduced to permit alignment of the TVFPN sequences.
See this image and copyright information in PMC

References

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